First published online September 25, 2003; 10.1104/pp.103.023499
Plant Physiology 133:653-663 (2003)
© 2003 American Society of Plant Biologists
DEVELOPMENT AND HORMONE ACTION
Expression and Maintenance of Embryogenic Potential Is Enhanced through Constitutive Expression of AGAMOUS-Like 151
Ellen W. Harding,
Weining Tang,
Karl W. Nichols2,
Donna E. Fernandez and
Sharyn E. Perry*
Department of Agronomy, University of Kentucky, 1405 Veterans Drive, Lexington, Kentucky 40546–0312 (E.W.H., W.T., S.E.P.); and Department of Botany, University of Wisconsin, 430 Lincoln Drive, Madison, Wisconsin 53706–1381 (K.W.N., D.E.F.)
The MADS domain protein AGL15 (AGAMOUS-Like 15) has been found to preferentially accumulate in angiosperm tissues derived from double fertilization (i.e. the embryo, suspensor, and endosperm) and in apomictic, somatic, and microspore embryos. Localization to the nuclei supports a role in gene regulation during this phase of the life cycle. To test whether AGL15 is involved in the promotion and maintenance of embryo identity, the embryogenic potential of transgenic plants that constitutively express AGL15 was assessed. Expression of AGL15 was found to enhance production of secondary embryos from cultured zygotic embryos, and constitutive expression led to long-term maintenance of development in this mode. Ectopic accumulation of AGL15 also promoted somatic embryo formation after germination from the shoot apical meristem of seedlings in culture. These results indicate that AGL15 is involved in support of development in an embryonic mode.
Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.103.023499.
1 This work was supported by the National Science Foundation (grant no. IBN–9984274 to S.E.P.), by the U.S. Department of Agriculture (grant no. 96–35304–3699 to D.E.F.), by the University of Wisconsin Graduate School, and by the University of Kentucky. This paper (no. 03–06–036) is published with the approval of the Director of the Kentucky Agricultural Experiment Station.
2 Present address: Third Wave Technologies, Inc., 502 S. Rosa Road, Madison, WI 53719–1256.
* Corresponding author; e-mail sperr2{at}uky.edu; fax 859–257–7125.
Received March 14, 2003;
returned for revision May 6, 2003;
accepted July 1, 2003.
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